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Glucose-6-phosphate dehydrogenase increases Ca²⁺ currents by interacting with Ca_v1.2 and reducing intrinsic inactivation of the L-type calcium channel.

ABSTRACT: Pyridine nucleotides, such as NADPH and NADH, are emerging as critical players in the regulation of heart and vascular function. Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme in the pentose phosphate pathway, is the primary source and regulator of cellular NADPH. In the current study, we have identified two isoforms of G6PD (slow and fast migrating) and functionally characterized the slow migrating isoform of G6PD (G6PD₅₄₅) in bovine and human arteries. We found that G6PD₅₄₅ is eluted in the caveolae fraction of vascular smooth muscle (VSM) and has a higher maximum rate of reaction (V_max: 1.65-fold) than its fast migrating isoform (G6PD₅₁₅). Interestingly, caveolae G6PD forms a complex with the pore-forming α_1C

SUBMITTER: Gupte R

PROVIDER: S-EPMC7474437 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Dataset Information

Glucose-6-phosphate dehydrogenase increases Ca²⁺ currents by interacting with Ca_v1.2 and reducing intrinsic inactivation of the L-type calcium channel.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Glucose-6-phosphate dehydrogenase increases Ca2+ currents by interacting with Cav1.2 and reducing intrinsic inactivation of the L-type calcium channel.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Glucose-6-phosphate dehydrogenase increases Ca²⁺ currents by interacting with Ca_v1.2 and reducing intrinsic inactivation of the L-type calcium channel.